Chaperonins: two rings for folding

Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a basic functional mechanism. Although a large amount of information has been gathered for the simpler group I, much less i...

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Bibliographic Details
Published inTrends in biochemical sciences (Amsterdam. Regular ed.) Vol. 36; no. 8; pp. 424 - 432
Main Authors Yébenes, Hugo, Mesa, Pablo, Muñoz, Inés G., Montoya, Guillermo, Valpuesta, José M.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.08.2011
Subjects
Archaea
Chaperonin Containing TCP-1 - chemistry
chaperonins
cytosol
electron microscopy
Eubacteria
Group I Chaperonins - chemistry
Group II Chaperonins - chemistry
groups
Humans
Models, Molecular
organelles
Protein Conformation
Protein Folding
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Summary:Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a basic functional mechanism. Although a large amount of information has been gathered for the simpler group I, much less is known about group II chaperonins. Recent crystallographic and electron microscopy structures have provided new insights into the mechanism of these chaperonins and revealed important differences between group I and II chaperonins, mainly in the molecular rearrangements that take place during the functional cycle. These differences are evident for the most complex chaperonin, the eukaryotic cytosolic CCT, which highlights the uniqueness of this important molecular machine.
Bibliography:http://dx.doi.org/10.1016/j.tibs.2011.05.003
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ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2011.05.003